Publications of Research Area Z3
Microscopy core facility and antibody production: Analysis of protease structure, cell biology and function
Teilprojektleiter: Paul Saftig / Joachim Grötzinger
- The disintegrin domain of ADAM17 antagonises fibroblast-carcinoma cell interactions.
Trad, A., Riese, M., Shomali, M., Hedeman, N. Grötzinger, J., Lorenzen, I.
Int J Oncol 42, 1793-1800 (2013) - ADAM17-overexpressing breast cancer cells selectively targeted by antibody-toxin conjugate. Trad, A., Hansen, H.P., Shomali, M., Peipp, M., Klausz, K., Hedemann, N., Yamamoto, K., Desel, C., Lorenzen, I., Lemke, H., Rose-John, S., Grötzinger, J. Cancer Immunology Immunotherapy 62, 411-421 (2013)
- A novel bispecific single-chain antibody for ADAM17 and CD3 induces T-cell-mediated lysis of prostate cancer cells. Yamamoto K, Trad A, Baumgart A, Hüske L, Lorenzen I, Chalaris A, Grötzinger J, Dechow T, Scheller J, Rose-John S. Biochem J. 2012 Jul 1;445(1):135-44.
- Immunoglobulin class switching appears to be regulated by B-cell antigen receptor-specific T-cell action. Lange H, Hecht O, Zemlin M, Trad A, Tanasa RI, Schroeder HW Jr, Lemke H. Eur J Immunol. 2012 Apr;42(4):1016-29.
- The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II. Lorenzen I, Lokau J, Düsterhöft S, Trad A, Garbers C, Scheller J, Rose-John S, Grötzinger J. FEBS Lett. 2012 Apr 24;586(8):1093-100.
- Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain. Lorenzen I, Trad A, Grötzinger J. Biochem Biophys Res Commun. 2011 Nov 18;415(2):330-6.
- Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17.Trad A, Hedemann N, Shomali M, Pawlak V, Grötzinger J, Lorenzen I.J Immunol Methods. 2011 Aug 31;371(1-2):91-6
